Amylase alpha 1A (salivary) (AMY1A)

Amylase alpha 1A (salivary) (AMY1A) is a secreted calcium-binding enzyme produced primarily by the human salivary glands that catalyzes the hydrolysis of internal (1→4)-alpha-D-glucoside bonds in starch and glycogen, yielding maltose, maltotriose, dextrins, and small amounts of glucose[2][4]. This enzyme is the major contributor to the initial digestion of carbohydrates in the oral cavity. It is encoded by the AMY1A gene, which exists in multiple copy number variations in human populations—a feature that correlates with dietary starch consumption and may influence both metabolic homeostasis and oral health[5][2]. Beyond its digestive role, salivary amylase activity is increasingly recognized as a sensitive, dynamic biomarker of autonomic nervous system activity, rising in response to psychosocial stress and physical exercise[2]. Copy number variation of AMY1A has been linked to individual variation in enzyme activity and to health outcomes such as obesity, cognitive function, Alzheimer's disease risk, and susceptibility to dental caries via modulating the oral microbiome[2]. AMY1A is not considered a classical therapeutic target in drug development but is of major interest for nutritional genomics, biomarker research, and human evolutionary biology[5][2][4].

Other names

Alpha-amylase 1AAMY11,4-alpha-D-glucan glucanohydrolase 1Salivary alpha-amylaseGlycogenaseAmylase, salivary, alpha-1ASalivary amylase alpha 1A

Not applicable (not a current drug target); enzyme catalyzes hydrolysis of internal 1,4-alpha-D-glucosidic bonds in polysaccharides[4]